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Volumn 104, Issue 11, 2013, Pages 2456-2464

Kinesin-8 is a low-force motor protein with a weakly bound slip state

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; KIF18A PROTEIN, HUMAN; KINESIN; KIP3 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84878886853     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.02.040     Document Type: Article
Times cited : (48)

References (51)
  • 1
    • 0035146128 scopus 로고    scopus 로고
    • The spindle: A dynamic assembly of microtubules and motors
    • T. Wittmann, A. Hyman, and A. Desai The spindle: a dynamic assembly of microtubules and motors Nat. Cell Biol. 3 2001 E28 E34
    • (2001) Nat. Cell Biol. , vol.3
    • Wittmann, T.1    Hyman, A.2    Desai, A.3
  • 2
    • 27844440885 scopus 로고    scopus 로고
    • Length control of the metaphase spindle
    • G. Goshima, and R. Wollman R.D. Vale Length control of the metaphase spindle Curr. Biol. 15 2005 1979 1988
    • (2005) Curr. Biol. , vol.15 , pp. 1979-1988
    • Goshima, G.1    Wollman, R.2    Vale, R.D.3
  • 3
    • 46049112667 scopus 로고    scopus 로고
    • Kinesin-8 molecular motors: Putting the brakes on chromosome oscillations
    • M.K. Gardner, D.J. Odde, and K. Bloom Kinesin-8 molecular motors: putting the brakes on chromosome oscillations Trends Cell Biol. 18 2008 307 310
    • (2008) Trends Cell Biol. , vol.18 , pp. 307-310
    • Gardner, M.K.1    Odde, D.J.2    Bloom, K.3
  • 4
    • 33748136479 scopus 로고    scopus 로고
    • Yeast kinesin-8 depolymerizes microtubules in a length-dependent manner
    • V. Varga, and J. Helenius J. Howard Yeast kinesin-8 depolymerizes microtubules in a length-dependent manner Nat. Cell Biol. 8 2006 957 962
    • (2006) Nat. Cell Biol. , vol.8 , pp. 957-962
    • Varga, V.1    Helenius, J.2    Howard, J.3
  • 5
    • 33748158378 scopus 로고    scopus 로고
    • Plus end-specific depolymerase activity of Kip3, a kinesin-8 protein, explains its role in positioning the yeast mitotic spindle
    • M.L. Gupta Jr., and P. Carvalho D. Pellman Plus end-specific depolymerase activity of Kip3, a kinesin-8 protein, explains its role in positioning the yeast mitotic spindle Nat. Cell Biol. 8 2006 913 923
    • (2006) Nat. Cell Biol. , vol.8 , pp. 913-923
    • Gupta, Jr.M.L.1    Carvalho, P.2    Pellman, D.3
  • 6
    • 70149111601 scopus 로고    scopus 로고
    • Kinesin-8 motors act cooperatively to mediate length-dependent microtubule depolymerization
    • V. Varga, and C. Leduc J. Howard Kinesin-8 motors act cooperatively to mediate length-dependent microtubule depolymerization Cell 138 2009 1174 1183
    • (2009) Cell , vol.138 , pp. 1174-1183
    • Varga, V.1    Leduc, C.2    Howard, J.3
  • 7
    • 67649389978 scopus 로고    scopus 로고
    • Microtubule depolymerization by the Kinesin-8 motor Kip3p: A mathematical model
    • L.E. Hough, and A. Schwabe M.D. Betterton Microtubule depolymerization by the Kinesin-8 motor Kip3p: a mathematical model Biophys. J. 96 2009 3050 3064
    • (2009) Biophys. J. , vol.96 , pp. 3050-3064
    • Hough, L.E.1    Schwabe, A.2    Betterton, M.D.3
  • 8
    • 33947111858 scopus 로고    scopus 로고
    • The human kinesin Kif18A is a motile microtubule depolymerase essential for chromosome congression
    • M.I. Mayr, and S. Hümmer T.U. Mayer The human kinesin Kif18A is a motile microtubule depolymerase essential for chromosome congression Curr. Biol. 17 2007 488 498
    • (2007) Curr. Biol. , vol.17 , pp. 488-498
    • Mayr, M.I.1    Hümmer, S.2    Mayer, T.U.3
  • 9
    • 76749091008 scopus 로고    scopus 로고
    • The kinesin-8 Kif18A dampens microtubule plus-end dynamics
    • Y. Du, C.A. English, and R. Ohi The kinesin-8 Kif18A dampens microtubule plus-end dynamics Curr. Biol. 20 2010 374 380
    • (2010) Curr. Biol. , vol.20 , pp. 374-380
    • Du, Y.1    English, C.A.2    Ohi, R.3
  • 10
    • 77958487248 scopus 로고    scopus 로고
    • Insight into the molecular mechanism of the multitasking kinesin-8 motor
    • C. Peters, and K. Brejc C.A. Moores Insight into the molecular mechanism of the multitasking kinesin-8 motor EMBO J. 29 2010 3437 3447
    • (2010) EMBO J. , vol.29 , pp. 3437-3447
    • Peters, C.1    Brejc, K.2    Moores, C.A.3
  • 11
    • 80755176813 scopus 로고    scopus 로고
    • A non-motor microtubule binding site is essential for the high processivity and mitotic function of kinesin-8 Kif18A
    • M.I. Mayr, and M. Storch T.U. Mayer A non-motor microtubule binding site is essential for the high processivity and mitotic function of kinesin-8 Kif18A PLoS ONE 6 2011 e27471
    • (2011) PLoS ONE , vol.6 , pp. 27471
    • Mayr, M.I.1    Storch, M.2    Mayer, T.U.3
  • 12
    • 80052187303 scopus 로고    scopus 로고
    • Mechanisms underlying the dual-mode regulation of microtubule dynamics by Kip3/kinesin-8
    • X. Su, and W. Qiu D. Pellman Mechanisms underlying the dual-mode regulation of microtubule dynamics by Kip3/kinesin-8 Mol. Cell 43 2011 751 763
    • (2011) Mol. Cell , vol.43 , pp. 751-763
    • Su, X.1    Qiu, W.2    Pellman, D.3
  • 13
    • 80052230972 scopus 로고    scopus 로고
    • A tethering mechanism controls the processivity and kinetochore- microtubule plus-end enrichment of the kinesin-8 Kif18A
    • J. Stumpff, and Y. Du R. Ohi A tethering mechanism controls the processivity and kinetochore-microtubule plus-end enrichment of the kinesin-8 Kif18A Mol. Cell 43 2011 764 775
    • (2011) Mol. Cell , vol.43 , pp. 764-775
    • Stumpff, J.1    Du, Y.2    Ohi, R.3
  • 14
    • 38849201167 scopus 로고    scopus 로고
    • The kinesin-8 motor Kif18A suppresses kinetochore movements to control mitotic chromosome alignment
    • J. Stumpff, and G. von Dassow L. Wordeman The kinesin-8 motor Kif18A suppresses kinetochore movements to control mitotic chromosome alignment Dev. Cell 14 2008 252 262
    • (2008) Dev. Cell , vol.14 , pp. 252-262
    • Stumpff, J.1    Von Dassow, G.2    Wordeman, L.3
  • 15
    • 80052209594 scopus 로고    scopus 로고
    • Kif18A uses a microtubule binding site in the tail for plus-end localization and spindle length regulation
    • L.N. Weaver, and S.C. Ems-McClung C.E. Walczak Kif18A uses a microtubule binding site in the tail for plus-end localization and spindle length regulation Curr. Biol. 21 2011 1500 1506
    • (2011) Curr. Biol. , vol.21 , pp. 1500-1506
    • Weaver, L.N.1    Ems-Mcclung, S.C.2    Walczak, C.E.3
  • 16
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • R.D. Vale, and T. Funatsu T. Yanagida Direct observation of single kinesin molecules moving along microtubules Nature 380 1996 451 453
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Yanagida, T.3
  • 17
    • 68949208665 scopus 로고    scopus 로고
    • Protein friction limits diffusive and directed movements of kinesin motors on microtubules
    • V. Bormuth, and V. Varga E. Schäffer Protein friction limits diffusive and directed movements of kinesin motors on microtubules Science 325 2009 870 873
    • (2009) Science , vol.325 , pp. 870-873
    • Bormuth, V.1    Varga, V.2    Schäffer, E.3
  • 18
    • 0020453536 scopus 로고
    • Evidence for cross-bridge attachment in relaxed muscle at low ionic strength
    • B. Brenner, and M. Schoenberg E. Eisenberg Evidence for cross-bridge attachment in relaxed muscle at low ionic strength Proc. Natl. Acad. Sci. USA 79 1982 7288 7291
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 7288-7291
    • Brenner, B.1    Schoenberg, M.2    Eisenberg, E.3
  • 19
    • 75749090448 scopus 로고    scopus 로고
    • Coordination and collective properties of molecular motors: Theory
    • T. Guérin, and J. Prost J.F. Joanny Coordination and collective properties of molecular motors: theory Curr. Opin. Cell Biol. 22 2010 14 20
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 14-20
    • Guérin, T.1    Prost, J.2    Joanny, J.F.3
  • 20
    • 49449107340 scopus 로고    scopus 로고
    • Visualizing one-dimensional diffusion of proteins along DNA
    • J. Gorman, and E.C. Greene Visualizing one-dimensional diffusion of proteins along DNA Nat. Struct. Mol. Biol. 15 2008 768 774
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 768-774
    • Gorman, J.1    Greene, E.C.2
  • 21
    • 33646950699 scopus 로고    scopus 로고
    • The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends
    • J. Helenius, and G. Brouhard J. Howard The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends Nature 441 2006 115 119
    • (2006) Nature , vol.441 , pp. 115-119
    • Helenius, J.1    Brouhard, G.2    Howard, J.3
  • 22
    • 37649004096 scopus 로고    scopus 로고
    • XMAP215 is a processive microtubule polymerase
    • G.J. Brouhard, and J.H. Stear A.A. Hyman XMAP215 is a processive microtubule polymerase Cell 132 2008 79 88
    • (2008) Cell , vol.132 , pp. 79-88
    • Brouhard, G.J.1    Stear, J.H.2    Hyman, A.A.3
  • 23
    • 49749107045 scopus 로고    scopus 로고
    • Microtubule cross-linking triggers the directional motility of kinesin-5
    • L.C. Kapitein, and B.H. Kwok E.J. Peterman Microtubule cross-linking triggers the directional motility of kinesin-5 J. Cell Biol. 182 2008 421 428
    • (2008) J. Cell Biol. , vol.182 , pp. 421-428
    • Kapitein, L.C.1    Kwok, B.H.2    Peterman, E.J.3
  • 24
    • 60749102596 scopus 로고    scopus 로고
    • The diffusive interaction of microtubule binding proteins
    • J.R. Cooper, and L. Wordeman The diffusive interaction of microtubule binding proteins Curr. Opin. Cell Biol. 21 2009 68 73
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 68-73
    • Cooper, J.R.1    Wordeman, L.2
  • 25
    • 51149117363 scopus 로고    scopus 로고
    • Optical trapping of coated microspheres
    • V. Bormuth, and A. Jannasch E. Schäffer Optical trapping of coated microspheres Opt. Express 16 2008 13831 13844
    • (2008) Opt. Express , vol.16 , pp. 13831-13844
    • Bormuth, V.1    Jannasch, A.2    Schäffer, E.3
  • 26
    • 33947388331 scopus 로고    scopus 로고
    • LED illumination for video-enhanced DIC imaging of single microtubules
    • V. Bormuth, J. Howard, and E. Schäffer LED illumination for video-enhanced DIC imaging of single microtubules J. Microsc. 226 2007 1 5
    • (2007) J. Microsc. , vol.226 , pp. 1-5
    • Bormuth, V.1    Howard, J.2    Schäffer, E.3
  • 27
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • S.M. Block, L.S. Goldstein, and B.J. Schnapp Bead movement by single kinesin molecules studied with optical tweezers Nature 348 1990 348 352
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.2    Schnapp, B.J.3
  • 28
    • 34147198324 scopus 로고    scopus 로고
    • Surface forces and drag coefficients of microspheres near a plane surface measured with optical tweezers
    • E. Schäffer, S.F. Nørrelykke, and J. Howard Surface forces and drag coefficients of microspheres near a plane surface measured with optical tweezers Langmuir 23 2007 3654 3665
    • (2007) Langmuir , vol.23 , pp. 3654-3665
    • Schäffer, E.1    Nørrelykke, S.F.2    Howard, J.3
  • 29
    • 33750527817 scopus 로고    scopus 로고
    • Calibration of optical tweezers with positional detection in the back focal plane
    • S.F. Tolić-Nørrelykke, and E. Schäffer H. Flyvbjerg Calibration of optical tweezers with positional detection in the back focal plane Rev. Sci. Instrum. 77 2006 103101
    • (2006) Rev. Sci. Instrum. , vol.77 , pp. 103101
    • Tolić-Nørrelykke, S.F.1    Schäffer, E.2    Flyvbjerg, H.3
  • 30
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • K. Svoboda, and S.M. Block Force and velocity measured for single kinesin molecules Cell 77 1994 773 784
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 31
    • 0028843342 scopus 로고
    • The force generated by a single kinesin molecule against an elastic load
    • E. Meyhöfer, and J. Howard The force generated by a single kinesin molecule against an elastic load Proc. Natl. Acad. Sci. USA 92 1995 574 578
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 574-578
    • Meyhöfer, E.1    Howard, J.2
  • 33
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • K. Svoboda, and C.F. Schmidt S.M. Block Direct observation of kinesin stepping by optical trapping interferometry Nature 365 1993 721 727
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Block, S.M.3
  • 34
    • 0036112531 scopus 로고    scopus 로고
    • On the relation between noise spectra and the distribution of time between steps for single molecular motors
    • G. Charvin, D. Bensimon, and V. Croquette On the relation between noise spectra and the distribution of time between steps for single molecular motors Single Mol. 3 2002 43 48
    • (2002) Single Mol. , vol.3 , pp. 43-48
    • Charvin, G.1    Bensimon, D.2    Croquette, V.3
  • 35
    • 0035934881 scopus 로고    scopus 로고
    • Molecular motors: Thermodynamics and the random walk
    • N. Thomas, Y. Imafuku, and K. Tawada Molecular motors: thermodynamics and the random walk Proc. Biol. Sci. 268 2001 2113 2122
    • (2001) Proc. Biol. Sci. , vol.268 , pp. 2113-2122
    • Thomas, N.1    Imafuku, Y.2    Tawada, K.3
  • 37
    • 0037133038 scopus 로고    scopus 로고
    • Direct long-term observation of kinesin processivity at low load
    • J. Yajima, and M.C. Alonso Y.Y. Toyoshima Direct long-term observation of kinesin processivity at low load Curr. Biol. 12 2002 301 306
    • (2002) Curr. Biol. , vol.12 , pp. 301-306
    • Yajima, J.1    Alonso, M.C.2    Toyoshima, Y.Y.3
  • 38
    • 70350011897 scopus 로고    scopus 로고
    • Force and premature binding of ADP can regulate the processivity of individual Eg5 dimers
    • M.T. Valentine, and S.M. Block Force and premature binding of ADP can regulate the processivity of individual Eg5 dimers Biophys. J. 97 2009 1671 1677
    • (2009) Biophys. J. , vol.97 , pp. 1671-1677
    • Valentine, M.T.1    Block, S.M.2
  • 39
    • 33744987629 scopus 로고    scopus 로고
    • Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro
    • M.T. Valentine, and P.M. Fordyce S.M. Block Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro Nat. Cell Biol. 8 2006 470 476
    • (2006) Nat. Cell Biol. , vol.8 , pp. 470-476
    • Valentine, M.T.1    Fordyce, P.M.2    Block, S.M.3
  • 41
    • 77953762901 scopus 로고    scopus 로고
    • Regulation of a heterodimeric kinesin-2 through an unprocessive motor domain that is turned processive by its partner
    • M. Brunnbauer, and F. Mueller-Planitz Z. Okten Regulation of a heterodimeric kinesin-2 through an unprocessive motor domain that is turned processive by its partner Proc. Natl. Acad. Sci. USA 107 2010 10460 10465
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 10460-10465
    • Brunnbauer, M.1    Mueller-Planitz, F.2    Okten, Z.3
  • 42
    • 0037183926 scopus 로고    scopus 로고
    • Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization
    • M. Tomishige, D.R. Klopfenstein, and R.D. Vale Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization Science 297 2002 2263 2267
    • (2002) Science , vol.297 , pp. 2263-2267
    • Tomishige, M.1    Klopfenstein, D.R.2    Vale, R.D.3
  • 43
    • 84863451332 scopus 로고    scopus 로고
    • The highly processive kinesin-8, Kip3, switches microtubule protofilaments with a bias toward the left
    • V. Bormuth, and B. Nitzsche S. Diez The highly processive kinesin-8, Kip3, switches microtubule protofilaments with a bias toward the left Biophys. J 103 2012 L4 L6
    • (2012) Biophys. J , vol.103
    • Bormuth, V.1    Nitzsche, B.2    Diez, S.3
  • 44
    • 33747624954 scopus 로고    scopus 로고
    • Allosteric inhibition of kinesin-5 modulates its processive directional motility
    • B.H. Kwok, and L.C. Kapitein T.M. Kapoor Allosteric inhibition of kinesin-5 modulates its processive directional motility Nat. Chem. Biol. 2 2006 480 485
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 480-485
    • Kwok, B.H.1    Kapitein, L.C.2    Kapoor, T.M.3
  • 45
    • 79953285218 scopus 로고    scopus 로고
    • Directional switching of the kinesin Cin8 through motor coupling
    • J. Roostalu, and C. Hentrich T. Surrey Directional switching of the kinesin Cin8 through motor coupling Science 332 2011 94 99
    • (2011) Science , vol.332 , pp. 94-99
    • Roostalu, J.1    Hentrich, C.2    Surrey, T.3
  • 46
    • 83555164602 scopus 로고    scopus 로고
    • Directionality of individual kinesin-5 Cin8 motors is modulated by loop 8, ionic strength and microtubule geometry
    • A. Gerson-Gurwitz, and C. Thiede L. Gheber Directionality of individual kinesin-5 Cin8 motors is modulated by loop 8, ionic strength and microtubule geometry EMBO J. 30 2011 4942 4954
    • (2011) EMBO J. , vol.30 , pp. 4942-4954
    • Gerson-Gurwitz, A.1    Thiede, C.2    Gheber, L.3
  • 47
    • 70350425612 scopus 로고    scopus 로고
    • Diffusive movement of processive kinesin-1 on microtubules
    • H. Lu, and M.Y. Ali K.M. Trybus Diffusive movement of processive kinesin-1 on microtubules Traffic 10 2009 1429 1438
    • (2009) Traffic , vol.10 , pp. 1429-1438
    • Lu, H.1    Ali, M.Y.2    Trybus, K.M.3
  • 48
    • 34347375813 scopus 로고    scopus 로고
    • Load-dependent release limits the processive stepping of the tetrameric Eg5 motor
    • M.J. Korneev, S. Lakämper, and C.F. Schmidt Load-dependent release limits the processive stepping of the tetrameric Eg5 motor Eur. Biophys. J. 36 2007 675 681
    • (2007) Eur. Biophys. J. , vol.36 , pp. 675-681
    • Korneev, M.J.1    Lakämper, S.2    Schmidt, C.F.3
  • 49
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
    • Y. Okada, and N. Hirokawa Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin Proc. Natl. Acad. Sci. USA 97 2000 640 645
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2


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